| |  Online-Ressource |
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| Verfasst von: | Miller, Stephanie Barbara Maria [VerfasserIn]  |
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| | Ho, Chi-Ting [VerfasserIn] |
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| | Winkler, Juliane [VerfasserIn] |
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| | Khokhrina, Maria [VerfasserIn] |
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| | Neuner, Annett [VerfasserIn] |
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| | Richter, Karsten [VerfasserIn] |
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| | Schiebel, Elmar [VerfasserIn] |
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| | Mogk, Axel [VerfasserIn] |
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| | Bukau, Bernd [VerfasserIn] |
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| Titel: | Compartment-specific aggregases direct distinct nuclear and cytoplasmic aggregate deposition |
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| Verf.angabe: | Stephanie BM Miller, Chi-Ting Ho, Juliane Winkler, Maria Khokhrina, Annett Neuner, Mohamed YH Mohamed, D Lys Guilbride, Karsten Richter, Michael Lisby, Elmar Schiebel, Axel Mogk & Bernd Bukau |
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| E-Jahr: | 2015 |
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| Jahr: | 11 February 2015 |
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| Umfang: | 20 S. |
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| Fussnoten: | Gesehen am 08.06.2020 |
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| Titel Quelle: | Enthalten in: European Molecular Biology OrganizationThe EMBO journal |
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| Ort Quelle: | Heidelberg : EMBO Press, 1982 |
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| Jahr Quelle: | 2015 |
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| Band/Heft Quelle: | 34(2015), 6, Seite 778-797 |
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| ISSN Quelle: | 1460-2075 |
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| Abstract: | Abstract Disruption of the functional protein balance in living cells activates protective quality control systems to repair damaged proteins or sequester potentially cytotoxic misfolded proteins into aggregates. The established model based on Saccharomyces cerevisiae indicates that aggregating proteins in the cytosol of eukaryotic cells partition between cytosolic juxtanuclear (JUNQ) and peripheral deposits. Substrate ubiquitination acts as the sorting principle determining JUNQ deposition and subsequent degradation. Here, we show that JUNQ unexpectedly resides inside the nucleus, defining a new intranuclear quality control compartment, INQ, for the deposition of both nuclear and cytosolic misfolded proteins, irrespective of ubiquitination. Deposition of misfolded cytosolic proteins at INQ involves chaperone-assisted nuclear import via nuclear pores. The compartment-specific aggregases, Btn2 (nuclear) and Hsp42 (cytosolic), direct protein deposition to nuclear INQ and cytosolic (CytoQ) sites, respectively. Intriguingly, Btn2 is transiently induced by both protein folding stress and DNA replication stress, with DNA surveillance proteins accumulating at INQ. Our data therefore reveal a bipartite, inter-compartmental protein quality control system linked to DNA surveillance via INQ and Btn2. |
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| DOI: | doi:10.15252/embj.201489524 |
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| URL: | Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.
Volltext ; Verlag: https://doi.org/10.15252/embj.201489524 |
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| | Volltext: https://www.embopress.org/doi/full/10.15252/embj.201489524 |
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| | DOI: https://doi.org/10.15252/embj.201489524 |
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| Datenträger: | Online-Ressource |
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| Sprache: | eng |
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| Sach-SW: | chaperones |
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| | protein aggregation |
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| | protein disaggregation |
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| | proteostasis |
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| | ubiquitin-proteasome system |
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| K10plus-PPN: | 1700131737 |
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| Verknüpfungen: | → Zeitschrift |
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Compartment-specific aggregases direct distinct nuclear and cytoplasmic aggregate deposition / Miller, Stephanie Barbara Maria [VerfasserIn]; 11 February 2015 (Online-Ressource)
